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PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) in plants: regulations and functions

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Title PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) in plants: regulations and functions
 
Creator Kamble, Nitin Uttam
Majee, Manoj
 
Subject abiotic stress
isoaspartyl
protein damage
protein l-isoaspartyl methyltransferase
protein repair
seed
 
Description Accepted date: November 10 2020
Proteins are essential molecules that carry out key functions in a cell. However, as a result of aging or stressful environments, the protein undergoes a range of spontaneous covalent modifications, including the formation of abnormal l-isoaspartyl residues from aspartyl or asparaginyl residues, which can disrupt the protein's inherent structure and function. PROTEIN l-ISOASPARTYL METHYLTRANSFERASE (PIMT: EC 2.1.1.77), an evolutionarily conserved ancient protein repairing enzyme (PRE), converts such abnormal l-isoaspartyl residues to normal l-aspartyl residues and re-establishes the protein's native structure and function. Although originally discovered in animals as a PRE, PIMT emerged as a key PRE in plants, particularly in seeds, in which PIMT plays a predominant role in preserving seed vigor and viability for prolonged periods of time. Interestingly, higher plants encode a second PIMT (PIMT2) protein which possesses a unique N-terminal extension, and exhibits several distinct features and far more complexity than non-plant PIMTs. Recent studies indicate that the role of PIMT is not restricted to preserving seed vigor and longevity but is also implicated in enhancing the growth and survivability of plants under stressful environments. Furthermore, expression studies indicate the tantalizing possibility that PIMT is involved in various physiological processes apart from its role in seed vigor, longevity and plant's survivability under abiotic stress. This review article particularly describes new insights and emerging interest in all facets of this enzyme in plants along with a concise comparative overview on isoAsp formation, and the role and regulation of PIMTs across evolutionary diverse species. Additionally, recent methods and their challenges in identifying isoaspartyl containing proteins (PIMT substrates) are highlighted.
 
Date 2020-12-01T09:50:00Z
2020-12-01T09:50:00Z
2020
 
Type Article
 
Identifier Biochemical Journal, 477(22): 4453-4471
1470-8728
https://doi.org/10.1042/BCJ20200794
https://portlandpress.com/biochemj/article-abstract/477/22/4453/227075/PROTEIN-l-ISOASPARTYL-METHYLTRANSFERASE-PIMT-in?redirectedFrom=fulltext
http://223.31.159.10:8080/jspui/handle/123456789/1129
 
Language en_US
 
Publisher Portland Press